GenomeNet

Database: UniProt
Entry: Q71VZ1
LinkDB: Q71VZ1
Original site: Q71VZ1 
ID   GSHAB_LISMF             Reviewed;         769 AA.
AC   Q71VZ1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   05-DEC-2018, entry version 85.
DE   RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000255|HAMAP-Rule:MF_00782};
DE   AltName: Full=Gamma-GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE            Short=GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE   Includes:
DE     RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00782};
DE              EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GCS {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE   Includes:
DE     RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE              EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00782};
GN   Name=gshAB {ECO:0000255|HAMAP-Rule:MF_00782};
GN   Synonyms=gshF {ECO:0000255|HAMAP-Rule:MF_00782};
GN   OrderedLocusNames=LMOf2365_2760;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
CC       via gamma-L-glutamyl-L-cysteine. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
CC         glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +
CC         glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00782};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00782}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC       cysteine ligase type 1 family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00782}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT05525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE017262; AAT05525.1; ALT_INIT; Genomic_DNA.
DR   ProteinModelPortal; Q71VZ1; -.
DR   SMR; Q71VZ1; -.
DR   EnsemblBacteria; AAT05525; AAT05525; LMOf2365_2760.
DR   KEGG; lmf:LMOf2365_2760; -.
DR   HOGENOM; HOG000156471; -.
DR   KO; K01919; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00782; Glut_biosynth; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006335; Glut_biosynth.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   PANTHER; PTHR38761; PTHR38761; 2.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 2.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01435; glu_cys_lig_rel; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding.
FT   CHAIN         1    769       Glutathione biosynthesis bifunctional
FT                                protein GshAB.
FT                                /FTId=PRO_0000192554.
FT   DOMAIN      514    768       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00782}.
FT   NP_BIND     541    599       ATP. {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   REGION        1    347       Glutamate--cysteine ligase.
FT   METAL       721    721       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       738    738       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       738    738       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       740    740       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
SQ   SEQUENCE   769 AA;  87751 MW;  94140E0923FCD379 CRC64;
     MLDSFKEDPK LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN PYIKTDFSES
     QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN PPILPAEEDI PIAEYKTPDS
     PDRKYREHLA KGYGKKIQLL SGIHYNFSFP EALIDGLYDK ISLPEESKQD FKNRLYLKVA
     KYFMKNRWLL IYLTGASPVY LADFSKTKHD ESLPDGSSAL RDGISLRNSN AGYKNKEALY
     VDYNSFDAYI SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAEHG VEYLEIRSID
     LNPLESNGIS KDELAFIHLF LIKGLLSEDR ELCSNNQQLA DENENNIALN GLAQPALKNC
     DNEEISVVEA GLLELNKMSD FIQSLRPEDT KLQAIIEKQK ERLLHPEKTI AAQVKQQVTK
     EGYVDFHLNQ AKTYMEETEA LAYKLIGAED MELSTQIIWK DAIARGIKVD VLDRAENFLR
     FQKGDHVEYV KQASKTSKDN YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF
     SLFEDKQIVV KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF
     LVINDKVEAV LKRVPANVTG DGIHTVRELV EEKNTDPLRG TDHLKPLEKI RTGPEETLML
     SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD YFKEIAIRAT QVLDAKICGV
     DIIVPRETID RDKHAIIELN FNPAMHMHCF PYQGEKKKIG DKILDFLFE
//
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